PRLR_RABIT
ID PRLR_RABIT Reviewed; 616 AA.
AC P14787;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Prolactin receptor;
DE Short=PRL-R;
DE Flags: Precursor;
GN Name=PRLR;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RX PubMed=2928321; DOI=10.1073/pnas.86.6.2112;
RA Edery M., Jolicoeur C., Levi-Meyrueis C., Dusanter-Fourt I., Petridou B.,
RA Boutin J.-M., Lesueur L., Kelly P.A., Djiane J.;
RT "Identification and sequence analysis of a second form of prolactin
RT receptor by molecular cloning of complementary DNA from rabbit mammary
RT gland.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:2112-2116(1989).
RN [2]
RP PROTEIN SEQUENCE OF 41-66; 90-108; 150-201 AND 277-285.
RX PubMed=2289615; DOI=10.1016/0020-711x(90)90106-d;
RA Waters M.J., Spencer S.A., Hamlin G., Henzel W.J., Wood W.I.;
RT "Purification and partial sequence of the rabbit mammary gland prolactin
RT receptor.";
RL Int. J. Biochem. 22:1089-1095(1990).
RN [3]
RP 3D-STRUCTURE MODELING OF 23-228.
RX PubMed=9094747;
RX DOI=10.1002/(sici)1097-0134(199703)27:3<459::aid-prot13>3.0.co;2-k;
RA Halaby D., Thoreau E., Djiane J., Mornon J.-P.;
RT "Homology modeling of rabbit prolactin hormone complexed with its
RT receptor.";
RL Proteins 27:459-468(1997).
CC -!- FUNCTION: This is a receptor for the anterior pituitary hormone
CC prolactin.
CC -!- SUBUNIT: Interacts with SMARCA1. Interacts with NEK3 and VAV2 and this
CC interaction is prolactin-dependent. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
CC folding and thereby efficient intracellular transport and cell-surface
CC receptor binding.
CC -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC activation.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 1
CC subfamily. {ECO:0000305}.
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DR EMBL; J04510; AAA31457.1; -; mRNA.
DR PIR; A30304; A30304.
DR RefSeq; NP_001075700.1; NM_001082231.1.
DR RefSeq; XP_017199967.1; XM_017344478.1.
DR RefSeq; XP_017199969.1; XM_017344480.1.
DR RefSeq; XP_017199970.1; XM_017344481.1.
DR RefSeq; XP_017199971.1; XM_017344482.1.
DR RefSeq; XP_017199972.1; XM_017344483.1.
DR RefSeq; XP_017199973.1; XM_017344484.1.
DR AlphaFoldDB; P14787; -.
DR SMR; P14787; -.
DR STRING; 9986.ENSOCUP00000004567; -.
DR PRIDE; P14787; -.
DR Ensembl; ENSOCUT00000005269; ENSOCUP00000004567; ENSOCUG00000005274.
DR GeneID; 100009046; -.
DR KEGG; ocu:100009046; -.
DR CTD; 5618; -.
DR eggNOG; ENOG502R22A; Eukaryota.
DR GeneTree; ENSGT00940000154851; -.
DR HOGENOM; CLU_017892_2_0_1; -.
DR InParanoid; P14787; -.
DR OMA; YHYELRL; -.
DR OrthoDB; 346239at2759; -.
DR TreeFam; TF330851; -.
DR Proteomes; UP000001811; Chromosome 11.
DR Bgee; ENSOCUG00000005274; Expressed in liver and 15 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004925; F:prolactin receptor activity; IEA:InterPro.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR015152; Growth/epo_recpt_lig-bind.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003528; Long_hematopoietin_rcpt_CS.
DR InterPro; IPR033230; PRLR.
DR PANTHER; PTHR23036:SF86; PTHR23036:SF86; 2.
DR Pfam; PF09067; EpoR_lig-bind; 1.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS01352; HEMATOPO_REC_L_F1; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Membrane;
KW Metal-binding; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Zinc.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..616
FT /note="Prolactin receptor"
FT /id="PRO_0000010980"
FT TOPO_DOM 25..234
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..616
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..128
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 129..229
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 326..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 215..219
FT /note="WSXWS motif"
FT MOTIF 267..275
FT /note="Box 1 motif"
FT COMPBIAS 335..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..46
FT /evidence="ECO:0000250"
FT DISULFID 75..86
FT /evidence="ECO:0000250"
FT CONFLICT 106
FT /note="T -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="G -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="D -> F (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 616 AA; 68840 MW; 800E3166FEF7108C CRC64;
MKENVASMIV FLLLLFLNIR LLKGQSPPGK PFIFKCRSPE KETFTCWWRP GADGGLPTNY
TLTYHKEGET ITHECPDYKT GGPNSCYFSK KHTSIWTIYI ITVNATNQMG SSVSDPRYVD
VTYIVEPDPP VNLTLEVKHP EDRKPYLWVK WLPPTLVDVR SGWLTLQYEI RLKPEKAAEW
ETHFAGQQTQ FKILSLYPGQ KYLVQVRCKP DHGFWSVWSP ESSIQIPNDF TMKDITVWIF
VAVLSTIICL IMVWAVALKG YSMVTCIFPP VPGPKIKGFD THLLEKGKSE ELLSAFGCQD
FPPTADCEDL LVEFLEVDDS EDQQLMPAHS KEHSGPGMKP TDLDPDNDSG RGSCDSPSLL
SEKCEEPQAN PSTFHTPEVI EQPEKPKANV THTWDPQTIS LVGKMPYLSV NGSKSSTWPL
LQPGQHNTNS PYHNIADMCK LATSLDKIDK DALQSSKTTE AAGEEKATKQ REVESSHSKA
EQDTGWLLPK EKPPFISPKP LDYVEIHKVN KDGALSLLLK QKENGDQTGK AGTPETSKEY
AKVSRVMDNN ILVLVQDPGA QNVALFEEST KEAPPSPSQN QAEKDLSSFS TAPSDCRLQQ
GGLDYLDPAC FMHSLH
